3GTO
Backtracked RNA polymerase II complex with 15mer RNA
Summary for 3GTO
Entry DOI | 10.2210/pdb3gto/pdb |
Related | 3GTG 3GTJ 3GTK 3GTL 3GTM 3GTP 3GTQ |
Descriptor | DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC4, RNA (5'-R(*AP*UP*CP*GP*AP*GP*AP*GP*GP*AP*UP*GP*CP*AP*C)-3'), ... (15 entities in total) |
Functional Keywords | transcription, transferase, dna-rna hybrid, backtrack, dna-directed rna polymerase, dna binding, isopeptide bond, magnesium, metal binding, nucleotidyltransferase, nucleus, phosphoprotein, zinc-finger, dna damage, dna repair, transferase-dna-rna hybrid complex, transferase/dna-rna hybrid |
Biological source | Saccharomyces cerevisiae (yeast) More |
Cellular location | Nucleus: P04050 P08518 P16370 P20434 P20436 P27999 P38902 Nucleus, nucleolus: P40422 P22139 Cytoplasm: P20435 |
Total number of polymer chains | 13 |
Total formula weight | 487849.84 |
Authors | Wang, D.,Bushnell, D.A.,Huang, X.,Westover, K.D.,Levitt, M.,Kornberg, R.D. (deposition date: 2009-03-27, release date: 2009-06-09, Last modification date: 2024-10-30) |
Primary citation | Wang, D.,Bushnell, D.A.,Huang, X.,Westover, K.D.,Levitt, M.,Kornberg, R.D. Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution. Science, 324:1203-1206, 2009 Cited by PubMed Abstract: Transcribing RNA polymerases oscillate between three stable states, two of which, pre- and posttranslocated, were previously subjected to x-ray crystal structure determination. We report here the crystal structure of RNA polymerase II in the third state, the reverse translocated, or "backtracked" state. The defining feature of the backtracked structure is a binding site for the first backtracked nucleotide. This binding site is occupied in case of nucleotide misincorporation in the RNA or damage to the DNA, and is termed the "P" site because it supports proofreading. The predominant mechanism of proofreading is the excision of a dinucleotide in the presence of the elongation factor SII (TFIIS). Structure determination of a cocrystal with TFIIS reveals a rearrangement whereby cleavage of the RNA may take place. PubMed: 19478184DOI: 10.1126/science.1168729 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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